title: Redesign of the coenzyme specificity of a dehydrogenase by protein engineering.
abstract: Directed mutagenesis and molecular modelling have been used to identify a set of amino-acid side chains in glutathione reductase that confer specificity for the coenzyme NADP+. Systematic replacement of these amino acids, all of which occur in a 'fingerprint' structural motif in the NADP+-binding domain, leaves the substrate specificity unchanged but converts the enzyme into one displaying a marked preference for the coenzyme NAD+.
authors.affiliation: Department of Biochemistry, University of Cambridge, UK.
authors.forename: N S
authors.initials: NS
authors.lastname: Scrutton
authors.forename: A
authors.initials: A
authors.lastname: Berry
authors.forename: R N
authors.initials: RN
authors.lastname: Perham
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D003196:Computer Graphics; D004252:DNA Mutational Analysis; D005980:Glutathione Reductase / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009243:NAD / Q000378:metabolism*; D009249:NADP / Q000378:metabolism*; D015202:Protein Engineering; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
chemical_list: D009243:NAD; D009249:NADP; D005980:Glutathione Reductase